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分子伴侣BiP参与辛德毕斯病毒包膜糖蛋白的成熟过程。

Involvement of the molecular chaperone BiP in maturation of Sindbis virus envelope glycoproteins.

作者信息

Mulvey M, Brown D T

机构信息

Cell Research Institute, University of Texas at Austin 78713-7640.

出版信息

J Virol. 1995 Mar;69(3):1621-7. doi: 10.1128/JVI.69.3.1621-1627.1995.

Abstract

Sindbis virus codes for two membrane glycoproteins, E1 and PE2, which assemble into heterodimers within the endoplasmic reticulum. We have examined the role of the molecular chaperone BiP (grp78) in the maturation of these two proteins. E1, which folds into its mature conformation via at least three intermediates differing in the configurations of their disulfide bonds, was found to interact strongly and transiently with BiP after synthesis. ATP depletion mediated by carbonyl cyanide m-chlorophenylhydrazone treatment results in the stabilization of complexes between BiP and E1. The depletion of intracellular ATP levels also greatly inhibits conversions between the E1 folding intermediates and results in the slow incorporation of E1 into disulfide-stabilized aggregates. These results suggest that the ATP-regulated binding and release of BiP have a role in modulating disulfide bond formation during E1 folding. In comparison with E1, very little PE2 is normally recovered in association with BiP. However, under conditions in which E1 folding is aberrant, increased amounts of PE2 become directly associated with BiP. The formation of these BiP-PE2 interactions occurs after E1 begins to misfold or fails to fold efficiently. We propose that nascent PE2 is stable prior to pairing with E1 for only a limited period of time, after which unpaired PE2 becomes recognized by BiP. This implies that the productive association of PE2 and E1 must occur within a restricted time frame and only after E1 has accomplished certain folding steps mediated by BiP binding and release. Kinetic studies which show that the pairing of E1 with PE2 is delayed after translocation support this conclusion.

摘要

辛德毕斯病毒编码两种膜糖蛋白,即E1和PE2,它们在内质网中组装成异二聚体。我们研究了分子伴侣BiP(grp78)在这两种蛋白成熟过程中的作用。E1通过至少三种其二硫键构型不同的中间体折叠成成熟构象,发现其在合成后与BiP强烈且短暂地相互作用。羰基氰化物间氯苯腙处理介导的ATP消耗导致BiP与E1之间复合物的稳定。细胞内ATP水平的降低也极大地抑制了E1折叠中间体之间的转化,并导致E1缓慢掺入二硫键稳定的聚集体中。这些结果表明,BiP的ATP调节结合和释放对E1折叠过程中二硫键的形成具有调节作用。与E1相比,通常很少能回收与BiP结合的PE2。然而,在E1折叠异常的条件下,与BiP直接结合的PE2量增加。这些BiP-PE2相互作用在E1开始错误折叠或未能有效折叠后发生。我们提出,新生的PE2在与E1配对之前仅在有限的时间内是稳定的,之后未配对的PE2会被BiP识别。这意味着PE2和E1的有效结合必须在有限的时间框架内发生,并且仅在E1完成了由BiP结合和释放介导的某些折叠步骤之后。动力学研究表明,E1与PE2的配对在转运后延迟,这支持了这一结论。

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